Recombinant Golden hamster Il1a protein, His&Strep II-tagged
Cat.No. : | Il1a-4532G |
Product Overview : | Recombinant Golden hamster Il1a protein(A0A1U7Q4M0)(1-269aa), fused with N-terminal His tag and C-terminal Strep II tag, was expressed in E.coli. |
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Source : | E.coli |
Species : | Golden hamster |
Tag : | His&Strep II |
Protein length : | 1-269a.a. |
Form : | If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Molecular Mass : | 32.8 kDa |
AASequence : | MAKVPDLFEDLKNCYSENEEYNSAI DHLSLSQKSFYDASYGSLHENCTDK FVSLRTSETSKMSSLTFEESLVMVA ATSDKGKILKKRRLGFNQAFAEDDL ETITRNLEETIQSDSAPYVFQSNMR YKLIRRVMQEFVLNDSLNQNIYLDA DQVHLKAASLNDLQHEVKFDMYVYS SEDDSKYPVTLKISNTQLFVSAQGE DQPVLLKEMPEIPKVITGSETDLIF FWKTVNSKNYFTSAAYPELFIATKE QSQVHLAMGLPSMTDFQIS |
Purity : | Greater than 90% as determined by SDS-PAGE. |
Storage : | Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. |
Reconstitution : | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. |
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Not For Human Consumption!
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Customer Reviews (3)
Write a reviewHigh solubility.
Good for intracellular staining.
Effective in apoptosis assays.
Q&As (10)
Ask a questionCross-talk between IL-1α's and other cytokines is dissected through methods such as co-immunoprecipitation, ELISA, and cytokine profiling arrays.
IL-1α's paradoxical roles are dissected using conditional knockout mice, 3D culture systems, and molecular analyses to delineate context-specific effects.
Single-cell RNA sequencing uncovers heterogeneity in IL-1α-responsive cell populations and their roles, revealing distinct molecular profiles and functions.
IL-1α's intricate pro-inflammatory signaling pathways are decoded using advanced techniques like mass spectrometry, phosphoproteomics, and bioinformatics.
Genetic editing tools like CRISPR-Cas9 unveil IL-1α's contributions to diseases by generating knockout models and studying resulting phenotypic changes.
In vitro co-culture systems are manipulated to study IL-1α-mediated responses, elucidating immune-stromal cell interactions via cytokine-specific neutralization.
Specific cellular receptors and effectors influenced by IL-1α are identified through techniques like co-immunoprecipitation, ChIP-seq, and siRNA knockdown.
Live-cell microscopy captures real-time IL-1α release dynamics and its impact on neighboring cells, facilitated by fluorescent tagging and high-resolution imaging.
Longitudinal studies and statistical modeling establish the quantitative relationship between IL-1α levels and disease progression, offering predictive insights.
Multi-omics analyses provide a holistic view of IL-1α signaling's impact, integrating transcriptomics, proteomics, and metabolomics data for comprehensive insights.
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